ID A0A0D2N165_9CHLO Unreviewed; 688 AA.
AC A0A0D2N165;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Cell division protease FtsH {ECO:0000313|EMBL:KIZ06262.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:KIZ06262.1};
GN ORFNames=MNEG_1688 {ECO:0000313|EMBL:KIZ06262.1};
OS Monoraphidium neglectum.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX NCBI_TaxID=145388 {ECO:0000313|EMBL:KIZ06262.1, ECO:0000313|Proteomes:UP000054498};
RN [1] {ECO:0000313|EMBL:KIZ06262.1, ECO:0000313|Proteomes:UP000054498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIZ06262.1,
RC ECO:0000313|Proteomes:UP000054498};
RX PubMed=24373495; DOI=10.1186/1471-2164-14-926;
RA Bogen C., Al-Dilaimi A., Albersmeier A., Wichmann J., Grundmann M.,
RA Rupp O., Lauersen K.J., Blifernez-Klassen O., Kalinowski J., Goesmann A.,
RA Mussgnug J.H., Kruse O.;
RT "Reconstruction of the lipid metabolism for the microalga Monoraphidium
RT neglectum from its genome sequence reveals characteristics suitable for
RT biofuel production.";
RL BMC Genomics 14:926-926(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000256|ARBA:ARBA00010550}.
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DR EMBL; KK100394; KIZ06262.1; -; Genomic_DNA.
DR RefSeq; XP_013905281.1; XM_014049827.1.
DR AlphaFoldDB; A0A0D2N165; -.
DR STRING; 145388.A0A0D2N165; -.
DR MEROPS; M41.005; -.
DR GeneID; 25734566; -.
DR KEGG; mng:MNEG_1688; -.
DR OrthoDB; 94at2759; -.
DR Proteomes; UP000054498; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.720.210; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Cell cycle {ECO:0000313|EMBL:KIZ06262.1};
KW Cell division {ECO:0000313|EMBL:KIZ06262.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KIZ06262.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KIZ06262.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054498};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 155..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 246..385
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 688 AA; 73868 MW; 5B447182206A3CB1 CRC64;
MQALQQRAVA PARLSARPIP VGLARPRSVV VRAQQQQDVK PDGERRQFLT SVLTAAAALV
PAAAARAADD AAGVASSRMS YSRFLEYLDM GRVKKVDLYE NGTIAIVEAV SPELGNRVQR
VRVQLPGTSA ELLNKFREKK IDFAAHSNTE DGGAVFLNLL GNLAFPLLLV GGLFLLSRRS
GGGGMGGPGG NNPMAFGKSK ARFQMEPNTG VTFTDVAGVD EAKQDFMEIV EFLKRPERFT
AVGARIPKGC LLVGPPGTGK TLLAKAIAGE AGVPFFSISG SEFVEMFVGV GASRVRDLFK
KAKENAPCLV FVDEIDAVGR SRGTGIGGGN DEREQTLNQL LTEMDGFEGN TGIIVIAATN
RADILDPALL RPGRFDRQVT VDVPDQKGRL EILKVHARNK KLDGEVELQE VAMRTPGFAG
ADLANLLNEA AILAGRRGLT GIRNQEIDDA VDRIVAGMEG KPLTDGKAKQ LVAYHEVGHA
ICGTLTPGHD PVQKVTLIPR GQARGLTWFV PGEDPTLISK HQIFARIVGA LGGRAAEEVI
FGEAEVTSGA SGDLQQVTSM ARQMVINYGM SDIGPWSLMD PSAQGGDVVM RMMSRNSMSE
NLQRRIDEAV KQLSEQAYEV ALSQIRENRE AIDKIVEVLM EKETIGGNDF RAMLSEYTTI
PEENLKAVAE EATPALASAF EALDSEQL
//
